ID G7YGQ7_CLOSI Unreviewed; 947 AA.
AC G7YGQ7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Alpha-aminoadipic semialdehyde synthase {ECO:0000313|EMBL:GAA52140.1, ECO:0000313|EMBL:KAG5451549.1};
GN ORFNames=CLF_107394 {ECO:0000313|EMBL:GAA52140.1}, CSKR_104315
GN {ECO:0000313|EMBL:KAG5451549.1};
OS Clonorchis sinensis (Chinese liver fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Clonorchis.
OX NCBI_TaxID=79923 {ECO:0000313|EMBL:GAA52140.1, ECO:0000313|Proteomes:UP000008909};
RN [1] {ECO:0000313|EMBL:GAA52140.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Henan {ECO:0000313|EMBL:GAA52140.1};
RX PubMed=22023798; DOI=10.1186/gb-2011-12-10-r107;
RA Wang X., Chen W., Huang Y., Sun J., Men J., Liu H., Luo F., Guo L., Lv X.,
RA Deng C., Zhou C., Fan Y., Li X., Huang L., Hu Y., Liang C., Hu X., Xu J.,
RA Yu X.;
RT "The draft genome of the carcinogenic human liver fluke Clonorchis
RT sinensis.";
RL Genome Biol. 12:R107-R107(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Henan;
RA Wang X., Huang Y., Chen W., Liu H., Guo L., Chen Y., Luo F., Zhou W.,
RA Sun J., Mao Q., Liang P., Zhou C., Tian Y., Men J., Lv X., Huang L.,
RA Zhou J., Hu Y., Li R., Zhang F., Lei H., Li X., Hu X., Liang C., Xu J.,
RA Wu Z., Yu X.;
RT "The genome and transcriptome sequence of Clonorchis sinensis provide
RT insights into the carcinogenic liver fluke.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAG5451549.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Cs-k2 {ECO:0000313|EMBL:KAG5451549.1};
RX PubMed=29454982;
RA Wang D., Korhonen P.K., Gasser R.B., Young N.D.;
RT "Improved genomic resources and new bioinformatic workflow for the
RT carcinogenic parasite Clonorchis sinensis: Biotechnological implications.";
RL Biotechnol. Adv. 36:894-904(2018).
RN [4] {ECO:0000313|EMBL:KAG5451549.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Cs-k2 {ECO:0000313|EMBL:KAG5451549.1};
RX PubMed=33677057;
RA Young N.D., Stroehlein A.J., Kinkar L., Wang T., Sohn W.M., Chang B.C.H.,
RA Kaur P., Weisz D., Dudchenko O., Aiden E.L., Korhonen P.K., Gasser R.B.;
RT "High-quality reference genome for Clonorchis sinensis.";
RL Genomics 0:0-0(2021).
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 1/6.
CC {ECO:0000256|ARBA:ARBA00004682}.
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 2/6.
CC {ECO:0000256|ARBA:ARBA00004720}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the saccharopine
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00025744}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005624}.
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DR EMBL; DF143246; GAA52140.1; -; Genomic_DNA.
DR EMBL; NIRI02000042; KAG5451549.1; -; Genomic_DNA.
DR AlphaFoldDB; G7YGQ7; -.
DR STRING; 79923.G7YGQ7; -.
DR InParanoid; G7YGQ7; -.
DR UniPathway; UPA00868; UER00835.
DR Proteomes; UP000008909; Unassembled WGS sequence.
DR Proteomes; UP000286415; Chromosome 1.
DR GO; GO:0047131; F:saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0047130; F:saccharopine dehydrogenase (NADP+, L-lysine-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR CDD; cd12189; LKR_SDH_like; 1.
DR Gene3D; 1.10.1870.10; Domain 3, Saccharopine reductase; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032095; Sacchrp_dh-like_C.
DR InterPro; IPR005097; Sacchrp_dh_NADP.
DR PANTHER; PTHR11133:SF25; ALPHA-AMINOADIPIC SEMIALDEHYDE SYNTHASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11133; SACCHAROPINE DEHYDROGENASE; 1.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR Pfam; PF16653; Sacchrp_dh_C; 1.
DR Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008909}.
FT DOMAIN 38..172
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 212..416
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 947 AA; 105010 MW; B574C63A2BB0B6F5 CRC64;
MFARLSVPRL CMSGVCSTLH GTPRRSVNRA SLSRPVVGIK RETVNLWEQR SPLTPSQVHQ
LISQHGVRVL VQPSNRRCFT SSEYEAAGAE IAENLEDATL ILGVKRPAEL RPHDLLQDKT
YAFFTHTIKA QPANMTLLDT LFERNIRIID YECMVNEHNK RVVAFGQHAG MAGTIDIIHG
LGIRLLALGH RTPFMHVSIA HNYHNLNEAQ QAIRLVGYEL ALGRLPASIG PLVFVINGDG
NVAQGAEKIL NNLPAKSISP RELQHVANQG ETNVIYLCKV NPSHYMEHKD GKPFVEEEYF
RKPEDYKSNF INKIAPYTSV LINATYWDSR IDRILTRENV KSLIDVKPNV SGSPLNEACP
TLPYRMIAIC DISADSNGSI EFTDECTTID EPFVLYDPRT DKEKRTIAGD GILMCSIDNL
PAQLPFEASE HFGTALIPYL PDMVKSDATQ PFDRYNAGPV VKNAIIASNG ALTPKFQYID
SLRKKTGLSS TSTSSKKVLI LGAGYVVPPV IEYLSRDKSV ELTVVSNIYD ELSELARHYP
NILARNVNVL EDNQSLANLI QNSDLVLSLI PWRFHPTVVT ECVKQKRNLL TASYCTPNLK
EMESSIQQAG ITAVMEIGLD PGIDHLLTKE CIDDVRAKGG RVISYRSYTG GLPAPENSSN
PLRYKFSWSP EAALSTVMNG AKYLENGKIK EVPADGSLMK MASPMNLFPG FNLEGYPNRD
STRYIDLYGL TGCETVIRGT LRYSGYANAV LFMLDLGLLQ THQEAHLRPG AQKLSWRELI
CQKLGLHNQL TGNELRRAVL SKLEGNQAKY DCLNELGFLS DDTVAQAGTP LASTALQLSR
YLSYGPNERD LIIMAHELTI DWPDKKQREY RKVSLVAYGT AGQGKAGLAM SRTVGLPAAI
AAKMILDGEI TEKGIVLPLK PEIYKPILEK LKTEGIEAHE TSTFCDM
//